PGT2_LITER
ID PGT2_LITER Reviewed; 306 AA.
AC Q8W404;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=4-hydroxybenzoate geranyltransferase 2;
DE EC=2.5.1.93;
DE AltName: Full=PHB geranyltransferase 2;
DE Short=LePGT2;
GN Name=PGT-2;
OS Lithospermum erythrorhizon (Purple gromwell) (Lithospermum officinale var.
OS erythrorhizon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Boraginales; Boraginaceae; Boraginoideae; Lithospermeae;
OC Lithospermum.
OX NCBI_TaxID=34254;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11744717; DOI=10.1074/jbc.m106387200;
RA Yazaki K., Kunihisa M., Fujisaki T., Sato F.;
RT "Geranyl diphosphate:4-hydroxybenzoate geranyltransferase from Lithospermum
RT erythrorhizon. Cloning and characterization of a key enzyme in shikonin
RT biosynthesis.";
RL J. Biol. Chem. 277:6240-6246(2002).
RN [2]
RP SUBCELLULAR LOCATION.
RX DOI=10.1016/S0031-9422(00)95147-1;
RA Yamaga Y., Nakanishi K., Fukui H., Tabata M.;
RT "Intracellular localization of p-hydroxybenzoate geranyltransferase, a key
RT enzyme involved in shikonin biosynthesis.";
RL Phytochemistry 32:633-636(1993).
RN [3]
RP INDUCTION BY METHYL JASMONATE, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=9640665; DOI=10.1007/s004250050337;
RA Muehlenweg A., Melzer M., Li S.M., Heide L.;
RT "4-Hydroxybenzoate 3-geranyltransferase from Lithospermum erythrorhizon:
RT purification of a plant membrane-bound prenyltransferase.";
RL Planta 205:407-413(1998).
CC -!- FUNCTION: Prenyltransferase involved in the biosynthesis of shikonin, a
CC naphthoquinone secondary metabolite. Could accept only geranyl
CC diphosphate and not dimethylallyl diphosphate, farnesyl diphosphate, or
CC geranylgeranyl diphosphate as substrate. {ECO:0000269|PubMed:11744717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + 4-hydroxybenzoate = 3-geranyl-4-
CC hydroxybenzoate + diphosphate; Xref=Rhea:RHEA:27854,
CC ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:60878; EC=2.5.1.93;
CC Evidence={ECO:0000269|PubMed:11744717, ECO:0000269|PubMed:9640665};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9640665};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53.8 uM for 4-hydroxybenzoate {ECO:0000269|PubMed:11744717};
CC KM=45.9 uM for geranyl diphosphate {ECO:0000269|PubMed:11744717};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed only in roots.
CC {ECO:0000269|PubMed:11744717}.
CC -!- INDUCTION: Up-regulated in the dark and by methyl jasmonate or
CC oligogalacturonide. Down-regulated in the light and by ammonium or 2,4-
CC dichlorophenoxyacetic acid (2,4-D). {ECO:0000269|PubMed:11744717,
CC ECO:0000269|PubMed:9640665}.
CC -!- DOMAIN: The N-terminus (1-130) is determinant for the chain length
CC specificity. Region I (76-96) and region III (201-229) are involved in
CC the recognition of both substrates in a coordinated manner (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB055079; BAB84123.1; -; mRNA.
DR AlphaFoldDB; Q8W404; -.
DR SMR; Q8W404; -.
DR PRIDE; Q8W404; -.
DR KEGG; ag:BAB84123; -.
DR BRENDA; 2.5.1.93; 3048.
DR SABIO-RK; Q8W404; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0102930; F:4-hydroxybenzoate geranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0002094; F:polyprenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR006370; HB_polyprenyltransferase-like.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Magnesium; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..306
FT /note="4-hydroxybenzoate geranyltransferase 2"
FT /id="PRO_0000409381"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 306 AA; 34222 MW; 8C214E27589A791F CRC64;
MSSKQTQLKK GKQPSWIEIY LPKEVRPYAH LARLDKPIGS WLLAWPAFWS VALIADLGSL
PKMLAIFGWW AVWIRGAGCT INDYFDRDFD KKVERTKSRP LASGAVSPAK GLWWLAFQLF
IGLGVLYQFN ILTLALAIVH VPFVFAYPLM KRITYWPQAF LGVMISWGAL LGSSALKGSV
VPSIAYPLYI SSFFWTLVYD TIYAHQDKVD DAKAGIKSTA LRFGDATKIW ITWFGIGCIG
ALLLGGFIVN IGLPYYVFLA IATGQLIWQI FTVDLSSPMD CGKKFVSNQW FGAIIFTGIL
VGRLFP
